Analytical Data
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Gene name
AQP1
- Application
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Alternative Names
Aquaporin-CHIPUrine water channelWater channel protein for red blood cells and kidney proximal tubule
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P29972
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Expression Region
220-269aa
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Molecular Weight
32.6 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Aquaporin-1 (AQP1) is a water channel protein that plays a crucial role in water transport across cell membranes. It is predominantly expressed in kidney and erythrocyte cells, facilitating osmotic water flow and contributing to the regulation of body water homeostasis. Research into AQP1 has gained momentum due to its significant implications in various physiological and pathological conditions, including kidney function, brain edema, and cancer progression. The study of AQP1 and its recombinant forms allows for a deeper understanding of its structure-function relationship and its role in membrane biology. Recombinant AQP1 proteins can be produced in various systems, enabling the investigation of their biophysical properties, gating mechanisms, and interactions with other cellular components. Furthermore, AQP1 is also being explored as a potential therapeutic target for diseases characterized by dysregulated water transport, making its study increasingly relevant. By elucidating the molecular mechanisms underlying AQP1 function, researchers aim to identify novel strategies for clinical interventions, thereby advancing our knowledge in both basic and applied biomedical sciences.
